Sentences with phrase «lysine residues»
Lysine residues refer to specific parts of a molecule called lysine. Lysine is an amino acid, which is a building block of proteins. Residues are like individual units of lysine within a larger structure. So, when we talk about lysine residues, we are referring to the specific places where lysine is located in a protein or molecule. Full definition
Mammal sirtuins are NAD + - dependent deacetylases that use NAD + as cofactor for catalyzed reactions to cleave acetyl groups from acetylated lysine residues of target proteins, generating nicotinamide (NAM) and 2 ′ - O - acetyl - ADP - ribose.
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Brd4 forms complexes with chromatin via two tandem bromodomains (BD1 and BD2) that bind to acetylated lysine residues in histones and Brd4 association with acetylated chromatin is believed to regulate the recruitment of elongation factor b and additional transcription factors to specific promoter regions.
In previous research, Professor David Shreiber and his team functionalized lysine residues of type - I collagen with methacrylate groups to form collagen methacrylamide, or CMA.
The researchers found that propionyl and butyryl groups can be present on histone H3, specifically at lysine residue 14 (H3K14).
Methylation of arginine (Arg) and lysine residues in histones has been correlated with epigenetic forms of gene regulation.
These are somewhat confusingly named, but all of them indicate the addition of a methyl group (me) to a specific lysine residue (K) of histone H3, a key component of the nucleosome that undergoes various post-translation modifications.
Another important histone modification is acetylation (ac), which is the addition of an acetyl group to a lysine residue.
The simplest structure of glucosepane is a lysine residue linked to a arginine residue by a degraded form of glucose (which has turned into the imadazolium ring, etc).
This occurrence could have hindered the detection of junction - spanning peptides, since most mass spectrometry experiments involve digesting proteins with the enzyme trypsin, which cuts peptide chains exclusively after arginine and lysine residues.
He introduced a number of important techniques in chemical modification of proteins, in particular based on reversible amidination and trifluoroacetylation of lysine residues.
In addition, Pauling devised a clever yet simple method to address the issue of Lipoprotein (a) attaching to the lysine residues on the damaged collagen fibers in the arterial wall.